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Conformational dynamics of loops L11 and L12 of kinesin as revealed by spin-labeling EPR.

Abstract：

:The EPR spectra of the spin labels attached to loops L11 and L12 of kinesin were resolved into slow (rotational correlation time, tau=10-45 ns) and fast (tau=2 ns) components. The fraction of the slow component increased considerably when kinesin was complexed with a microtubule (MT). On MT binding and in the presence of nucleotides ADP and AMPPNP, the spin labels on L11, particularly at A252C and L249C, significantly decreased the fraction of the slow component. Moreover, dipolar EPR detected a wide distribution in distance range, 1-2 nm between the two spin labels attached to T242C/A252C or A247C/A252C; this distribution was slightly narrower in the presence of MTs than in their absence. These results suggested that the L11 residues undergo conformational transition on the binding of nucleotides and MT, while these residues remained to fluctuate over a nanometer range.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Yamada MD,Maruta S,Yasuda S,Kondo K,Maeda H,Arata T

doi

10.1016/j.bbrc.2007.10.043

subject

Has Abstract

pub_date

2007-12-21 00:00:00

pages

620-6

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(07)02213-9

journal_volume

364

pub_type

杂志文章

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